The conformational states of proteins are closely connected to their protonation states. A method to calculate the correlated population of protonation and conformational substates was developed, based on the concepts of statistical mechanics. The entropic contributions to dissoziation reactions were especially considered. Possible reorientations of dipolar or charged sidechains were modelled explicitly. Therefore, the stabilization of protonation states, resulting from the local relaxation of the protein sructure, is described. The method developed was succesfully applicated to the investigation of fluctuations in the groundstate and light induced relaxation of the Green Fluorescent Protein. Knowledge on the distribution of protonation states is important to be able to understand the photophysics of this protein. «

The conformational states of proteins are closely connected to their protonation states. A method to calculate the correlated population of protonation and conformational substates was developed, based on the concepts of statistical mechanics. The entropic contributions to dissoziation reactions were especially considered. Possible reorientations of dipolar or charged sidechains were modelled explicitly. Therefore, the stabilization of protonation states, resulting from the local relaxation of t... »